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Conserved domains on  [gi|6753320|ref|NP_033966|]
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T-complex protein 1 subunit gamma [Mus musculus]

Protein Classification

T-complex protein 1 subunit gamma( domain architecture ID 11494167)

T-complex protein 1 subunit gamma is a component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
6-529 0e+00

T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


:

Pssm-ID: 274085 [Multi-domain]  Cd Length: 524  Bit Score: 1003.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02344   1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02344  81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    166 SRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    326 ACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETG 485
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 6753320    486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
 
Name Accession Description Interval E-value
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
6-529 0e+00

T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274085 [Multi-domain]  Cd Length: 524  Bit Score: 1003.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02344   1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02344  81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    166 SRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    326 ACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETG 485
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 6753320    486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
6-525 0e+00

TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239453 [Multi-domain]  Cd Length: 480  Bit Score: 960.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03337   1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:cd03337  81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  166 SRWSSLACNIALDAVKTVQFEENGR-KEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSS 244
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGRkKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  245 LEYkkgesqtdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIA 324
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  325 RACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLD 404
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  405 PQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGET 484
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
                       490       500       510       520
                ....*....|....*....|....*....|....*....|.
gi 6753320  485 GTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSG 525
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
33-524 0e+00

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 578.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHF 112
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    113 LEQQMHPTVVISAYRMALDDMISTLKKI-STPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVqfeENGRK 191
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI---PKNDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    192 EIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQME 271
Cdd:pfam00118 158 SFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    272 EEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLE 351
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    352 IKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTG 431
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    432 VEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVE 511
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
                         490
                  ....*....|...
gi 6753320    512 TAVLLLRIDDIVS 524
Cdd:pfam00118 475 AASTILRIDDIIK 487
thermosome_alpha NF041082
thermosome subunit alpha;
6-524 0e+00

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 544.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041082   2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041082  82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   166 SRWSSLACNIALDAVKTVQfEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041082 162 EAAKDKLADLVVDAVKAVA-EKDGGYNVDL-DNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDG 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041082 399 KVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTG 477
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 6753320   486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041082 478 KVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
thermosome_beta NF041083
thermosome subunit beta;
6-524 0e+00

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 542.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041083   2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041083  82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   166 SRWSSLACNIALDAVKTVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041083 162 EEARDYLAEIAVKAVKQVAEKRDGKYYVDL-DNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTG 478
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 6753320   486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041083 479 EVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIA 517
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-533 6.76e-108

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 331.66  E-value: 6.76e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   19 GRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDG 94
Cdd:COG0459   8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDvnNREMMLSIINSSITTKvisrwSSLAcN 174
Cdd:COG0459  88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD-----EEIG-E 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  175 IALDAVKTVqfeengRKEIDIKkyarVEKiPGGIIEDSCVLRGVMINKDVTHP-------RMRRYIKNPRIVLLDSsley 247
Cdd:COG0459 160 LIAEAMEKV------GKDGVIT----VEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDK---- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  248 kkgesqtdiEITREEDFTRILqmeeeyihqlcEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRV-----------R 316
Cdd:COG0459 225 ---------KISSIQDLLPLL-----------EKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrR 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  317 KTDNNRIARACGARIVSR-----PEELREDDVGTgAGLLEikkIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNL 391
Cdd:COG0459 285 KAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRV 360
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  392 QDAMQVCRNVLLDpQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKht 471
Cdd:COG0459 361 EDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA-- 437
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753320  472 qeSCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQ 533
Cdd:COG0459 438 --KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
1-524 4.36e-97

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 304.64  E-value: 4.36e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     1 MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKmLLDPM------GGIVMTNDGNAILREIQVQH 74
Cdd:PTZ00212   2 IMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMsegprsGNVTVTNDGATILKSVWLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    75 PAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REM 151
Cdd:PTZ00212  81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   152 MLSIINSSITTKVISRWSSLACNIALDAVKTVqfeeNGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVThPRMRR 231
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKLAVDAVLRL----KGSGNLD---YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQPK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   232 YIKNPRIVLLDSSLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIHQLCEDIIQLKPDVVITEKGISDLAQHYL 304
Cdd:PTZ00212 233 RLENCKILVANTPMDTDK------IKIygakVKVDSMEKVAEIEAaekEKMKNKVDKILAHGCNVFINRQLIYNYPEQLF 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   305 MRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIkKIGDEYFTFITDCKDPKACTILLRGASKEIL 384
Cdd:PTZ00212 307 AEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAKGEACTIVLRGASTHIL 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   385 SEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLT 464
Cdd:PTZ00212 386 DEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVS 465
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   465 SLRAKHTQEScETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:PTZ00212 466 KLRAEHYKGN-KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
 
Name Accession Description Interval E-value
chap_CCT_gamma TIGR02344
T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the ...
6-529 0e+00

T-complex protein 1, gamma subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT gamma chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274085 [Multi-domain]  Cd Length: 524  Bit Score: 1003.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02344   1 PVLVLNQNTKRESGRKAQLSNIQAAKAVADIIRTCLGPRSMLKMLLDPMGGIVMTNDGNAILREIDVAHPAAKSMIELSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02344  81 TQDEEVGDGTTSVIILAGEMLSVAEPFLEQNIHPTVIIRAYRKALDDALSVLEEISIPVDVNDDAAMLKLIQSCIGTKFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    166 SRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:TIGR02344 161 SRWSDLMCDLALDAVRTVQRDENGRKEIDIKRYAKVEKIPGGDIEDSCVLKGVMINKDVTHPKMRRYIENPRIVLLDCPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:TIGR02344 241 EYKKGESQTNIEITKEEDWNRILQMEEEYVQLMCEDIIAVKPDLVITEKGVSDLAQHYLLKANITAIRRVRKTDNNRIAR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    326 ACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:TIGR02344 321 ACGATIVNRPEELRESDVGTGCGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDILNEVERNLQDAMAVARNVLLDP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETG 485
Cdd:TIGR02344 401 KLVPGGGATEMAVSVALTEKSKKLEGVEQWPYRAVADALEIIPRTLAQNCGANVIRTLTELRAKHAQENNCTWGIDGETG 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 6753320    486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:TIGR02344 481 KIVDMKEKGIWEPLAVKLQTYKTAIESACLLLRIDDIVSGVKKK 524
TCP1_gamma cd03337
TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved ...
6-525 0e+00

TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239453 [Multi-domain]  Cd Length: 480  Bit Score: 960.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03337   1 PVLVLNQNTKRESGRKAQLGNIQAAKTVADVIRTCLGPRAMLKMLLDPMGGIVLTNDGNAILREIDVAHPAAKSMIELSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:cd03337  81 TQDEEVGDGTTSVIILAGEILAVAEPFLERGIHPTVIIKAYRKALEDALKILEEISIPVDVNDRAQMLKIIKSCIGTKFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  166 SRWSSLACNIALDAVKTVQFEENGR-KEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSS 244
Cdd:cd03337 161 SRWSDLMCNLALDAVKTVAVEENGRkKEIDIKRYAKVEKIPGGEIEDSRVLDGVMLNKDVTHPKMRRRIENPRIVLLDCP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  245 LEYkkgesqtdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIA 324
Cdd:cd03337 241 LEY-----------------------------------------LVITEKGVSDLAQHYLVKAGITALRRVRKTDNNRIA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  325 RACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLD 404
Cdd:cd03337 280 RACGATIVNRPEELTESDVGTGAGLFEVKKIGDEYFTFITECKDPKACTILLRGASKDVLNEVERNLQDAMAVARNIILN 359
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  405 PQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGET 484
Cdd:cd03337 360 PKLVPGGGATEMAVSHALSEKAKSIEGVEQWPYKAVASALEVIPRTLAQNCGANVIRTLTELRAKHAQGENSTWGIDGET 439
                       490       500       510       520
                ....*....|....*....|....*....|....*....|.
gi 6753320  485 GTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSG 525
Cdd:cd03337 440 GDIVDMKELGIWDPLAVKAQTYKTAIEAACMLLRIDDIVSG 480
chaperonin_type_I_II cd00309
chaperonin families, type I and type II. Chaperonins are involved in productive folding of ...
14-524 0e+00

chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 238189  Cd Length: 464  Bit Score: 607.50  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd00309   1 KEREFGEEARLSNINAAKALADAVKTTLGPKGMDKMLVDSLGDPTITNDGATILKEIEVEHPAAKLLVEVAKSQDDEVGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd00309  81 GTTTVVVLAGELLKEAEKLLAAGIHPTEIIRGYEKAVEKALEILKEIAVPIDVEDREELLKVATTSLNSKLVSGGDDFLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  174 NIALDAVKTVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYkkgesq 253
Cdd:cd00309 161 ELVVDAVLKVGKENG----DVDLGVIRVEKKKGGSLEDSELVVGMVFDKGYLSPYMPKRLENAKILLLDCKLEY------ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  254 tdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd00309 231 -----------------------------------VVIAEKGIDDEALHYLAKLGIMAVRRVRKEDLERIAKATGATIVS 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  334 RPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd00309 276 RLEDLTPEDLGT-AGLVEETKIGDEKYTFIEGCKGGKVATILLRGATEVELDEAERSLHDALCAVRAAVEDGGIVPGGGA 354
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCeTWGVNGETGTLVDMKEL 493
Cdd:cd00309 355 AEIELSKALEELAKTLPGKEQLGIEAFADALEVIPRTLAENAGLDPIEVVTKLRAKHAEGGG-NAGGDVETGEIVDMKEA 433
                       490       500       510
                ....*....|....*....|....*....|.
gi 6753320  494 GIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd00309 434 GIIDPLKVKRQALKSATEAASLILTIDDIIV 464
Cpn60_TCP1 pfam00118
TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family ...
33-524 0e+00

TCP-1/cpn60 chaperonin family; This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.


Pssm-ID: 395068 [Multi-domain]  Cd Length: 489  Bit Score: 578.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHF 112
Cdd:pfam00118   1 LADIVRTSLGPKGMDKMLVNSGGDVTVTNDGATILKELEIQHPAAKLLVEAAKAQDEEVGDGTTTVVVLAGELLEEAEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    113 LEQQMHPTVVISAYRMALDDMISTLKKI-STPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVqfeENGRK 191
Cdd:pfam00118  81 LAAGVHPTTIIEGYEKALEKALEILDSIiSIPVEDVDREDLLKVARTSLSSKIISRESDFLAKLVVDAVLAI---PKNDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    192 EIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQME 271
Cdd:pfam00118 158 SFDLGN-IGVVKILGGSLEDSELVDGVVLDKGPLHPDMPKRLENAKVLLLNCSLEYEKTETKATVVLSDAEQLERFLKAE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    272 EEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLE 351
Cdd:pfam00118 237 EEQILEIVEKIIDSGVNVVVCQKGIDDLALHFLAKNGIMALRRVKKRDLERLAKATGARAVSSLDDLTPDDLGT-AGKVE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    352 IKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTG 431
Cdd:pfam00118 316 EEKIGDEKYTFIEGCKSPKAATILLRGATDHVLDEIERSIHDALCVVKNAIEDPRVVPGGGAVEMELARALREYAKSVSG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    432 VEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVE 511
Cdd:pfam00118 396 KEQLAIEAFAEALEVIPKTLAENAGLDPIEVLAELRAAH-ASGEKHAGIDVETGEIIDMKEAGVVDPLKVKRQALKSATE 474
                         490
                  ....*....|...
gi 6753320    512 TAVLLLRIDDIVS 524
Cdd:pfam00118 475 AASTILRIDDIIK 487
thermosome_alpha NF041082
thermosome subunit alpha;
6-524 0e+00

thermosome subunit alpha;


Pssm-ID: 469009  Cd Length: 518  Bit Score: 544.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041082   2 PILILKEGTQRTSGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDVVITNDGVTILKEMDIEHPAAKMIVEVAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041082  82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQDIHPTIIAEGYRLAAEKALEILDEIAIKVDPDDKETLKKIAATAMTGKGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   166 SRWSSLACNIALDAVKTVQfEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041082 162 EAAKDKLADLVVDAVKAVA-EKDGGYNVDL-DNIKVEKKVGGSIEDSELVEGVVIDKERVHPGMPKRVENAKIALLDAPL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041082 240 EVKKTEIDAKISITDPDQLQAFLDQEEKMLKEMVDKIADSGANVVFCQKGIDDLAQHYLAKEGILAVRRVKKSDMEKLAK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041082 320 ATGARIVTSIDDLSPEDLGY-AGLVEERKVGGDKMIFVEGCKNPKAVTILLRGGTEHVVDEVERALEDALRVVRVVLEDG 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041082 399 KVVAGGGAPEVELALRLREYAASVGGREQLAIEAFAEALEIIPRTLAENAGLDPIDALVELRSAH-EKGNKTAGLDVYTG 477
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 6753320   486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041082 478 KVVDMLEIGVVEPLRVKTQAIKSATEAAVMILRIDDVIA 516
thermosome_beta NF041083
thermosome subunit beta;
6-524 0e+00

thermosome subunit beta;


Pssm-ID: 469010  Cd Length: 519  Bit Score: 542.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:NF041083   2 PVLILKEGTQRTKGRDAQRNNIMAAKAVAEAVRTTLGPKGMDKMLVDSLGDIVITNDGATILKEMDVQHPAAKMLVEVAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:NF041083  82 TQDDEVGDGTTTAVVLAGELLKKAEELLDQNIHPTIIANGYRLAAEKAIEILDEIAEKVDPDDRETLKKIAETSLTSKGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   166 SRWSSLACNIALDAVKTVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSL 245
Cdd:NF041083 162 EEARDYLAEIAVKAVKQVAEKRDGKYYVDL-DNIQIEKKHGGSIEDTQLIYGIVIDKEVVHPGMPKRVENAKIALLDAPL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   246 EYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:NF041083 241 EVKKTEIDAEIRITDPDQLQKFLDQEEKMLKEMVDKIKATGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLAK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   326 ACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP 405
Cdd:NF041083 321 ATGARIVTNIDDLTPEDLGY-AELVEERKVGDDKMVFVEGCKNPKAVTILIRGGTEHVVDEAERALEDALSVVADAVEDG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   406 QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVNGETG 485
Cdd:NF041083 400 KIVAGGGAPEVELAKRLREYAATVGGREQLAVEAFAEALEIIPRTLAENAGLDPIDILVKLRSAH-EKGKKWAGINVFTG 478
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 6753320   486 TLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:NF041083 479 EVVDMWELGVIEPLRVKTQAIKSATEAATMILRIDDVIA 517
cpn60 cd03343
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They ...
7-524 0e+00

cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239459 [Multi-domain]  Cd Length: 517  Bit Score: 530.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    7 VLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03343   1 VLILKEGTQRTSGRDAQRMNIAAAKAVAEAVRTTLGPKGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVIS 166
Cdd:cd03343  81 QDEEVGDGTTTAVVLAGELLEKAEDLLDQNIHPTVIIEGYRLAAEKALELLDEIAIKVDPDDKDTLRKIAKTSLTGKGAE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  167 RWSSLACNIALDAVKTVQFEENGRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03343 161 AAKDKLADLVVDAVLQVAEKRDGKYVVDL-DNIKIEKKTGGSVDDTELIRGIVIDKEVVHPGMPKRVENAKIALLDAPLE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  247 YKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARA 326
Cdd:cd03343 240 VKKTEIDAKIRITSPDQLQAFLEQEEAMLKEMVDKIADTGANVVFCQKGIDDLAQHYLAKAGILAVRRVKKSDMEKLARA 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03343 320 TGAKIVTNIDDLTPEDLGE-AELVEERKVGDDKMVFVEGCKNPKAVTILLRGGTEHVVDELERALEDALRVVADALEDGK 398
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGETGT 486
Cdd:cd03343 399 VVAGGGAVEIELAKRLREYARSVGGREQLAVEAFADALEEIPRTLAENAGLDPIDTLVELRAAHEKGN-KNAGLDVYTGE 477
                       490       500       510
                ....*....|....*....|....*....|....*...
gi 6753320  487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03343 478 VVDMLEKGVIEPLRVKKQAIKSATEAATMILRIDDVIA 515
thermosome_arch TIGR02339
thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather ...
6-524 2.40e-176

thermosome, various subunits, archaeal; Thermosome is the name given to the archaeal rather than eukaryotic form of the group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacterial), a torroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins. Various homologous subunits, one to five per archaeal genome, may be designated alpha, beta, etc., but phylogenetic analysis does not show distinct alpha subunit and beta subunit lineages traceable to ancient paralogs. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274080  Cd Length: 519  Bit Score: 507.69  E-value: 2.40e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02339   1 PVFILKEGTQRTSGRDAQRNNIAAAKAVAEAVKSTLGPRGMDKMLVDSLGDVTITNDGATILKEMDIEHPAAKMLVEVAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVI 165
Cdd:TIGR02339  81 TQDEEVGDGTTTAVVLAGELLEKAEDLLEQDIHPTVIIEGYRKAAEKALEIIDEIATKISPEDRDLLKKIAYTSLTSKAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    166 SRWS-SLACNIALDAVKTV-QFEENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDS 243
Cdd:TIGR02339 161 AEVAkDKLADLVVEAVKQVaELRGDGKYYVDLDN-IKIVKKKGGSIEDTELVEGIVVDKEVVHPGMPKRVENAKIALLDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    244 SLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRI 323
Cdd:TIGR02339 240 PLEVEKTEIDAKIRITDPDQIKKFLDQEEAMLKEMVDKIASAGANVVICQKGIDDVAQHYLAKAGILAVRRVKKSDIEKL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    324 ARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLL 403
Cdd:TIGR02339 320 ARATGARIVSSIDEITESDLGY-AELVEERKVGEDKMVFVEGCKNPKAVTILLRGGTEHVVDELERSIQDALHVVANALE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    404 DPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGE 483
Cdd:TIGR02339 399 DGKIVAGGGAVEIELALRLRSYARSVGGREQLAIEAFADALEEIPRILAENAGLDPIDALVDLRAKHEKGN-KNAGINVF 477
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 6753320    484 TGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:TIGR02339 478 TGEIEDMLELGVIEPLRVKEQAIKSATEAATMILRIDDVIA 518
TCP1_epsilon cd03339
TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved ...
5-524 2.62e-128

TCP-1 (CTT or eukaryotic type II) chaperonin family, epsilon subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239455  Cd Length: 526  Bit Score: 385.11  E-value: 2.62e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    5 RPVLVL--SQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:cd03339   5 RPFIIVreQEKKKRLKGLEAHKSHILAAKSVANILRTSLGPRGMDKILVSPDGEVTVTNDGATILEKMDVDHQIAKLLVE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKIST--PVDVNNREMMLSIINSSI 160
Cdd:cd03339  85 LSKSQDDEIGDGTTGVVVLAGALLEQAEKLLDRGIHPIRIADGYEQACKIAVEHLEEIADkiEFSPDNKEPLIQTAMTSL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  161 TTKVISRWSSLACNIALDAVKTVQFEEngRKEID---IKkyarVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPR 237
Cdd:cd03339 165 GSKIVSRCHRQFAEIAVDAVLSVADLE--RKDVNfelIK----VEGKVGGRLEDTKLVKGIVIDKDFSHPQMPKEVKDAK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  238 IVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRK 317
Cdd:cd03339 239 IAILTCPFEPPKPKTKHKLDITSVEDYKKLQEYEQKYFREMVEQVKDAGANLVICQWGFDDEANHLLLQNGLPAVRWVGG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  318 TDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAM 395
Cdd:cd03339 319 VEIELIAIATGGRIVPRFEDLSPEKLGK-AGLVREISFGttKDKMLVIEGCPNSKAVTIFIRGGNKMIIEEAKRSLHDAL 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  396 QVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESC 475
Cdd:cd03339 398 CVVRNLIRDNRIVYGGGAAEISCSLAVEKAADKCSGIEQYAMRAFADALESIPLALAENSGLNPIETLSEVKARQVKEKN 477
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 6753320  476 ETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03339 478 PHLGIDCLGRGTNDMKEQKVFETLISKKQQILLATQVVKMILKIDDVIV 526
TCP1_delta cd03338
TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved ...
14-523 1.34e-125

TCP-1 (CTT or eukaryotic type II) chaperonin family, delta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239454 [Multi-domain]  Cd Length: 515  Bit Score: 377.78  E-value: 1.34e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   14 TKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGD 93
Cdd:cd03338   1 TDKEKPADVRLSNIQAAKAVADAIRTSLGPRGMDKMIQTGKGEVIITNDGATILKQMSVLHPAAKMLVELSKAQDIEAGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   94 GTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd03338  81 GTTSVVVLAGALLSACESLLKKGIHPTVISESFQIAAKKAVEILDSMSIPVDLNDRESLIKSATTSLNSKVVSQYSSLLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  174 NIALDAVKTVqFEENGRKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTH-PRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:cd03338 161 PIAVDAVLKV-IDPATATNVDLKDIRIVKKL-GGTIEDTELVDGLVFTQKASKkAGGPTRIEKAKIGLIQFCLSPPKTDM 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  253 QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANVTAIRRVRKTDNNRIARAC 327
Cdd:cd03338 239 DNNIVVNDYAQMDRILREERKYILNMCKKIKKSGCNVLLIQKSIlrdavSDLALHFLAKLKIMVVKDIEREEIEFICKTI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  328 GARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03338 319 GCKPVASIDHFTEDKLGS-ADLVEEVSLGDGKIVKITGVKNPgKTVTILVRGSNKLVLDEAERSLHDALCVIRCLVKKRA 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCeTWGVNGETGT 486
Cdd:cd03338 398 LIPGGGAPEIEIALQLSEWARTLTGVEQYCVRAFADALEVIPYTLAENAGLNPISIVTELRNRHAQGEK-NAGINVRKGA 476
                       490       500       510
                ....*....|....*....|....*....|....*..
gi 6753320  487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03338 477 ITNILEENVVQPLLVSTSAITLATETVRMILKIDDIV 513
TCP1_eta cd03340
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in ...
6-523 1.58e-123

TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239456 [Multi-domain]  Cd Length: 522  Bit Score: 372.78  E-value: 1.58e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:cd03340   1 PIILLKEGTDTSQGKGQLISNINACQAIADAVRTTLGPRGMDKLIVDGRGKVTISNDGATILKLLDIVHPAAKTLVDIAK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN----REMMLSIINSSIT 161
Cdd:cd03340  81 SQDAEVGDGTTSVVVLAGEFLKEAKPFIEDGVHPQIIIRGYRKALQLAIEKIKEIAVNIDKEDkeeqRELLEKCAATALN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  162 TKVISRWSSLACNIALDAVKTVQfEENGRKEIDIKKyarvekIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRI 238
Cdd:cd03340 161 SKLIASEKEFFAKMVVDAVLSLD-DDLDLDMIGIKK------VPGGSLEDSQLVNGVAFKKTFSyagFEQQPKKFKNPKI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  239 VLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKT 318
Cdd:cd03340 234 LLLNVELELKAEKDNAEVRVEDPEEYQAIVDAEWKIIYDKLEKIVKSGANVVLSKLPIGDLATQYFADRDIFCAGRVPEE 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  319 DNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:cd03340 314 DLKRVAQATGGSIQTTVSNITDDVLGT-CGLFEERQVGGERYNIFTGCPKAKTCTIILRGGAEQFIEEAERSLHDAIMIV 392
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETW 478
Cdd:cd03340 393 RRAIKNDSVVAGGGAIEMELSKYLRDYSRTIAGKQQLVINAFAKALEIIPRQLCDNAGFDATDILNKLRQKHAQGGGKWY 472
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*
gi 6753320  479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03340 473 GVDINNEGIADNFEAFVWEPSLVKINALTAATEAACLILSVDETI 517
chap_CCT_epsi TIGR02343
T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the ...
5-524 2.91e-122

T-complex protein 1, epsilon subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT epsilon chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274084 [Multi-domain]  Cd Length: 532  Bit Score: 369.90  E-value: 2.91e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      5 RPVLVLSQ--NTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIE 82
Cdd:TIGR02343   9 RPFIIIKDqdNKKRLKGLEAKKSNIAAAKSVASILRTSLGPKGMDKMLISPDGDITVTNDGATILSQMDVDNQIAKLMVE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     83 ISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPV--DVNNREMMLSIINSSI 160
Cdd:TIGR02343  89 LSKSQDDEIGDGTTGVVVLAGALLEQAEELLDKGIHPIKIADGFEEAARIAVEHLEEISDEIsaDNNNREPLIQAAKTSL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    161 TTKVISRWSSLACNIALDAVKTVQFEEngRKEIDIkKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVL 240
Cdd:TIGR02343 169 GSKIVSKCHRRFAEIAVDAVLNVADME--RRDVDF-DLIKVEGKVGGSLEDTKLIKGIIIDKDFSHPQMPKEVEDAKIAI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    241 LDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDN 320
Cdd:TIGR02343 246 LTCPFEPPKPKTKHKLDISSVEEYKKLQKYEQQKFKEMIDDIKKSGANLVICQWGFDDEANHLLLQNDLPAVRWVGGQEL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    321 NRIARACGARIVSRPEELREDDVGTgAGLLEIKKIG--DEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVC 398
Cdd:TIGR02343 326 ELIAIATGGRIVPRFQELSKDKLGK-AGLVREISFGttKDRMLVIEQCKNSKAVTIFIRGGNKMIIEEAKRSIHDALCVV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    399 RNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETW 478
Cdd:TIGR02343 405 RNLIKDSRIVYGGGAAEISCSLAVSQEADKYPGVEQYAIRAFADALETIPMALAENSGLDPIGTLSTLKSLQLKEKNPNL 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 6753320    479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:TIGR02343 485 GVDCLGYGTNDMKEQFVFETLIGKKQQILLATQLVRMILKIDDVIS 530
chap_CCT_eta TIGR02345
T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the ...
6-523 2.96e-121

T-complex protein 1, eta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274086 [Multi-domain]  Cd Length: 523  Bit Score: 366.78  E-value: 2.96e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      6 PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISR 85
Cdd:TIGR02345   3 TIVLLKEGTDTSQGKGQLISNINACVAIAEALKTTLGPRGMDKLIVGSNGKATISNDGATILKLLDIVHPAAKTLVDIAK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     86 TQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITT 162
Cdd:TIGR02345  83 SQDAEVGDGTTSVTILAGELLKEAKPFIEEGVHPQLIIRCYREALSLAVEKIKEIAVTIDEEKgeqRELLEKCAATALSS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    163 KVISRWSSLACNIALDAVKTVQFEENGRKEIDIKkyarveKIPGGIIEDSCVLRGVMINKDVT---HPRMRRYIKNPRIV 239
Cdd:TIGR02345 163 KLISHNKEFFSKMIVDAVLSLDRDDLDLKLIGIK------KVQGGALEDSQLVNGVAFKKTFSyagFEQQPKKFANPKIL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    240 LLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTD 319
Cdd:TIGR02345 237 LLNVELELKAEKDNAEIRVEDVEDYQAIVDAEWAIIFRKLEKIVESGANVVLSKLPIGDLATQYFADRDIFCAGRVSAED 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    320 NNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCR 399
Cdd:TIGR02345 317 LKRVIKACGGSIQSTTSDLEADVLGT-CALFEERQIGSERYNYFTGCPHAKTCTIILRGGAEQFIEEAERSLHDAIMIVR 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    400 NVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCetW- 478
Cdd:TIGR02345 396 RALKNKKIVAGGGAIEMELSKCLRDYSKTIDGKQQLIINAFAKALEIIPRQLCENAGFDSIEILNKLRSRHAKGGK--Wy 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 6753320    479 GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02345 474 GVDINTEDIGDNFEAFVWEPALVKINALKAAFEAACTILSVDETI 518
TCP1_alpha cd03335
TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved ...
15-523 1.10e-115

TCP-1 (CTT or eukaryotic type II) chaperonin family, alpha subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239451  Cd Length: 527  Bit Score: 352.74  E-value: 1.10e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:cd03335   2 ERTSGQDVRTQNVTAAMAIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDKEVGDG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK-ISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:cd03335  82 TTSVVIIAAELLKRANELVKQKIHPTTIISGYRLACKEAVKYIKEhLSISVDNLGKESLINVAKTSMSSKIIGADSDFFA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  174 NIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQ 253
Cdd:cd03335 162 NMVVDAILAVKTTNEKGKTKYPIKAVNILKAHGKSAKESYLVNGYALNCTRASQGMPTRVKNAKIACLDFNLQKTKMKLG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  254 TDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVS 333
Cdd:cd03335 242 VQVVVTDPEKLEKIRQRESDITKERIKKILAAGANVVLTTGGIDDMCLKYFVEAGAMAVRRVKKEDLRRIAKATGATLVS 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  334 RPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:cd03335 322 TLANLEGEETFDPSYLgeaeeVVQERIGDDELILIKGTKKRSSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSVV 401
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQESCETWGVN 481
Cdd:cd03335 402 PGGGAVETALSIYLENFATTLGSREQLAIAEFAEALLVIPKTLAVNAAKDATELVAKLRAYHaaaqvkpDKKHLKWYGLD 481
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 6753320  482 GETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03335 482 LINGKVRDNLEAGVLEPTVSKIKSLKFATEAAITILRIDDLI 523
chap_CCT_alpha TIGR02340
T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the ...
15-532 5.32e-115

T-complex protein 1, alpha subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274081 [Multi-domain]  Cd Length: 536  Bit Score: 351.33  E-value: 5.32e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     15 KRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDG 94
Cdd:TIGR02340   6 ERTSGQDVRTQNVTAAMAIANIVKTSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKILVELAQLQDREVGDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK-ISTPVDVNNREMMLSIINSSITTKVISRWSSLAC 173
Cdd:TIGR02340  86 TTSVVIIAAELLKRADELVKNKIHPTSVISGYRLACKEAVKYIKEnLSVSVDELGREALINVAKTSMSSKIIGLDSDFFS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    174 NIALDAVKTVQFE-ENGRKEIDIKKyARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGES 252
Cdd:TIGR02340 166 NIVVDAVLAVKTTnENGETKYPIKA-INILKAHGKSARESMLVKGYALNCTVASQQMPKRIKNAKIACLDFNLQKAKMAL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    253 QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIV 332
Cdd:TIGR02340 245 GVQIVVDDPEKLEQIRQREADITKERIKKILDAGANVVLTTGGIDDMCLKYFVEAGAMGVRRCKKEDLKRIAKATGATLV 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    333 SRPEELREDDVGTGAGL-----LEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQL 407
Cdd:TIGR02340 325 STLADLEGEETFEASYLgfadeVVQERIADDECILIKGTKKRKSASIILRGANDFMLDEMERSLHDALCVVKRTLESNSV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    408 VPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKH-------TQESCETWGV 480
Cdd:TIGR02340 405 VPGGGAVEAALSIYLENFATTLGSREQLAIAEFARALLIIPKTLAVNAAKDSTELVAKLRAYHaaaqlkpEKKHLKWYGL 484
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6753320    481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDD 532
Cdd:TIGR02340 485 DLVNGKIRDNKEAGVLEPTVSKVKSLKFATEAAITILRIDDLIKLNPEQSKG 536
chap_CCT_delta TIGR02342
T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the ...
16-523 3.59e-113

T-complex protein 1, delta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT delta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274083  Cd Length: 517  Bit Score: 346.00  E-value: 3.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     16 RESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGT 95
Cdd:TIGR02342   4 KDKPQDVRTSNIVAAKAVADAIRTSLGPKGMDKMIQDGKGEVIITNDGATILKQMAVLHPAAKMLVELSKAQDIEAGDGT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNI 175
Cdd:TIGR02342  84 TSVVILAGALLGACERLLNKGIHPTIISESFQSAADEAIKILDEMSIPVDLSDREQLLKSATTSLSSKVVSQYSSLLAPL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    176 ALDAVKTVQFEENGrKEIDIKKYARVEKIpGGIIEDSCVLRGVMINKDVTHPR-MRRYIKNPRIVLLDSSLEYKKGESQT 254
Cdd:TIGR02342 164 AVDAVLKVIDPENA-KNVDLNDIKVVKKL-GGTIDDTELIEGLVFTQKASKSAgGPTRIEKAKIGLIQFQISPPKTDMEN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    255 DIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGI-----SDLAQHYLMRANVTAIRRVRKTDNNRIARACGA 329
Cdd:TIGR02342 242 QIIVNDYAQMDRVLKEERAYILNIVKKIKKTGCNVLLIQKSIlrdavNDLALHFLAKMKIMVVKDIEREEIEFICKTIGC 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    330 RIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDP-KACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLV 408
Cdd:TIGR02342 322 KPIASIDHFTADKLGS-AELVEEVDSDGGKIIKITGIQNAgKTVTVVVRGSNKLVIDEAERSLHDALCVIRCLVKKRGLI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    409 PGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQEScETWGVNGETGTLV 488
Cdd:TIGR02342 401 AGGGAPEIEIARRLSKYARTMKGVESYCVRAFADALEVIPYTLAENAGLNPIKVVTELRNRHANGE-KTAGISVRKGGIT 479
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 6753320    489 DMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02342 480 NMLEEHVLQPLLVTTSAITLASETVRSILKIDDIV 514
GroEL COG0459
Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones]; ...
19-533 6.76e-108

Chaperonin GroEL (HSP60 family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440227  Cd Length: 497  Bit Score: 331.66  E-value: 6.76e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   19 GRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDG 94
Cdd:COG0459   8 GEDARRANIRGVKALADAVKVTLGPKGRNVMLVKSFGDPTITNDGVTIAKEIELEDPfenmGAQLVKEVASKTNDEAGDG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   95 TTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDvnNREMMLSIINSSITTKvisrwSSLAcN 174
Cdd:COG0459  88 TTTATVLAGALLKEGLKLVAAGANPTDIKRGIDKAVEKAVEELKKIAKPVD--DKEELAQVATISANGD-----EEIG-E 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  175 IALDAVKTVqfeengRKEIDIKkyarVEKiPGGIIEDSCVLRGVMINKDVTHP-------RMRRYIKNPRIVLLDSsley 247
Cdd:COG0459 160 LIAEAMEKV------GKDGVIT----VEE-GKGLETELEVVEGMQFDKGYLSPyfvtdpeKMPAELENAYILLTDK---- 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  248 kkgesqtdiEITREEDFTRILqmeeeyihqlcEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRV-----------R 316
Cdd:COG0459 225 ---------KISSIQDLLPLL-----------EKVAQSGKPLLIIAEDIDGEALATLVVNGIRGVLRVvavkapgfgdrR 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  317 KTDNNRIARACGARIVSR-----PEELREDDVGTgAGLLEikkIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNL 391
Cdd:COG0459 285 KAMLEDIAILTGGRVISEdlglkLEDVTLDDLGR-AKRVE---VDKDNTTIVEGAGNPKAIVILVGAATEVEVKERKRRV 360
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  392 QDAMQVCRNVLLDpQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKht 471
Cdd:COG0459 361 EDALHATRAAVEE-GIVPGGGAALLRAARALRELAAKLEGDEQLGIEIVARALEAPLRQIAENAGLDGSVVVEKVRAA-- 437
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753320  472 qeSCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQ 533
Cdd:COG0459 438 --KDKGFGFDAATGEYVDMLEAGVIDPAKVKRSALQNAASVAGLILTTEAVIADKPEKEEAA 497
TCP1_zeta cd03342
TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in ...
13-523 1.41e-104

TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239458 [Multi-domain]  Cd Length: 484  Bit Score: 322.67  E-value: 1.41e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAkSMIEISRT-QDE 89
Cdd:cd03342   2 NPKAEVLRRGQAlaVNISAAKGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLSEMQIQHPTA-SMIARAATaQDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   90 EVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDV-NNREMMLSIINSSITTKVISRW 168
Cdd:cd03342  81 ITGDGTTSNVLLIGELLKQAERYIQEGVHPRIITEGFELAKNKALKFLESFKVPVEIdTDRELLLSVARTSLRTKLHADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  169 SSLACNIALDAVKTVQFEEngrKEIDIKkyaRVE--KIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03342 161 ADQLTEIVVDAVLAIYKPD---EPIDLH---MVEimQMQHKSDSDTKLIRGLVLDHGARHPDMPKRVENAYILTCNVSLE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  247 YKKGESQTdieitreedftrilqmeeeyihqlcediiQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARA 326
Cdd:cd03342 235 YEKTEVNS-----------------------------GFFYSVVINQKGIDPPSLDMLAKEGILALRRAKRRNMERLTLA 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  327 CGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQ 406
Cdd:cd03342 286 CGGVAMNSVDDLSPECLGY-AGLVYERTLGEEKYTFIEGVKNPKSCTILIKGPNDHTITQIKDAIRDGLRAVKNAIEDKC 364
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  407 LVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCETWGVNGETGT 486
Cdd:cd03342 365 VVPGAGAFEVALYAHLKEFKKSVKGKAKLGVQAFADALLVIPKTLAENSGLDVQETLVKLQDEYA-EGGQVGGVDLDTGE 443
                       490       500       510
                ....*....|....*....|....*....|....*..
gi 6753320  487 LVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03342 444 PMDPESEGIWDNYSVKRQILHSATVIASQLLLVDEII 480
TCP1_theta cd03341
TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved ...
26-523 3.09e-103

TCP-1 (CTT or eukaryotic type II) chaperonin family, theta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239457 [Multi-domain]  Cd Length: 472  Bit Score: 318.78  E-value: 3.09e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03341  13 NIEACKELSQITRTSYGPNGMNKMVINHLEKLFVTSDAATILRELEVQHPAAKLLVMASQMQEEEIGDGTNLVVVLAGEL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKK--ISTPVDVNNREMMLSIINSSITTKVISRwSSLACNIALDAVKTV 183
Cdd:cd03341  93 LEKAEELLRMGLHPSEIIEGYEKALKKALEILEElvVYKIEDLRNKEEVSKALKTAIASKQYGN-EDFLSPLVAEACISV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKD----VTHprmrryIKNPRIVLLDSSLEykkgesqtdieit 259
Cdd:cd03341 172 LPENIGNFNVD---NIRVVKILGGSLEDSKVVRGMVFKREpegsVKR------VKKAKVAVFSCPFD------------- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  260 reedftrilqmeeeyihqlcediiqLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSR----- 334
Cdd:cd03341 230 -------------------------IGVNVIVAGGSVGDLALHYCNKYGIMVIKINSKFELRRLCRTVGATPLPRlgapt 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  335 PEELREDDVgtgaglLEIKKIGDEYFTFITDCK-DPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGA 413
Cdd:cd03341 285 PEEIGYCDS------VYVEEIGDTKVVVFRQNKeDSKIATIVLRGATQNILDDVERAIDDGVNVFKSLTKDGRFVPGAGA 358
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  414 SEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETwGVNGETG--TLVDMK 491
Cdd:cd03341 359 TEIELAKKLKEYGEKTPGLEQYAIKKFAEAFEVVPRTLAENAGLDATEVLSELYAAHQKGNKSA-GVDIESGdeGTKDAK 437
                       490       500       510
                ....*....|....*....|....*....|..
gi 6753320  492 ELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:cd03341 438 EAGIFDHLATKKWAIKLATEAAVTVLRVDQII 469
PTZ00212 PTZ00212
T-complex protein 1 subunit beta; Provisional
1-524 4.36e-97

T-complex protein 1 subunit beta; Provisional


Pssm-ID: 185514  Cd Length: 533  Bit Score: 304.64  E-value: 4.36e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     1 MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKmLLDPM------GGIVMTNDGNAILREIQVQH 74
Cdd:PTZ00212   2 IMANVPPQVLKQGAQEEKGETARLQSFVGAIAVADLVKTTLGPKGMDK-ILQPMsegprsGNVTVTNDGATILKSVWLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    75 PAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REM 151
Cdd:PTZ00212  81 PAAKILVDISKTQDEEVGDGTTSVVVLAGELLREAEKLLDQKIHPQTIIEGWRMALDVARKALEEIAFDHGSDEekfKED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   152 MLSIINSSITTKVISRWSSLACNIALDAVKTVqfeeNGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVThPRMRR 231
Cdd:PTZ00212 161 LLNIARTTLSSKLLTVEKDHFAKLAVDAVLRL----KGSGNLD---YIQIIKKPGGTLRDSYLEDGFILEKKIG-VGQPK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   232 YIKNPRIVLLDSSLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIHQLCEDIIQLKPDVVITEKGISDLAQHYL 304
Cdd:PTZ00212 233 RLENCKILVANTPMDTDK------IKIygakVKVDSMEKVAEIEAaekEKMKNKVDKILAHGCNVFINRQLIYNYPEQLF 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   305 MRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIkKIGDEYFTFITDCKDPKACTILLRGASKEIL 384
Cdd:PTZ00212 307 AEAGIMAIEHADFDGMERLAAALGAEIVSTFDTPEKVKLGHCDLIEEI-MIGEDKLIRFSGCAKGEACTIVLRGASTHIL 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   385 SEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLT 464
Cdd:PTZ00212 386 DEAERSLHDALCVLSQTVKDTRVVLGGGCSEMLMANAVEELAKKVEGKKSLAIEAFAKALRQIPTIIADNGGYDSAELVS 465
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   465 SLRAKHTQEScETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:PTZ00212 466 KLRAEHYKGN-KTAGIDMEKGTVGDMKELGITESYKVKLSQLCSATEAAEMILRVDDIIR 524
chap_CCT_zeta TIGR02347
T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the ...
13-523 5.40e-97

T-complex protein 1, zeta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT zeta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274088 [Multi-domain]  Cd Length: 531  Bit Score: 304.35  E-value: 5.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     13 NTKRESGRKVQS--GNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEE 90
Cdd:TIGR02347   6 NPKAESLRRDAAlmMNINAARGLQDVLKTNLGPKGTLKMLVSGAGDIKLTKDGNVLLNEMQIQHPTASMIARAATAQDDI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     91 VGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPV-DVNNREMMLSIINSSITTKVISRWS 169
Cdd:TIGR02347  86 TGDGTTSTVLLIGELLKQAERYILEGVHPRIITEGFEIARKEALQFLDKFKVKKeDEVDREFLLNVARTSLRTKLPADLA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    170 SLACNIALDAVKTVQFEEngrKEID---IKKYARVEKIPggiiEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:TIGR02347 166 DQLTEIVVDAVLAIKKDG---EDIDlfmVEIMEMKHKSA----TDTTLIRGLVLDHGARHPDMPRRVKNAYILTCNVSLE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    247 YKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLK-------PD---VVITEKGISDLAQHYLMRANVTAIRRVR 316
Cdd:TIGR02347 239 YEKTEVNSGFFYSSAEQREKLVKAERKFVDDRVKKIIELKkkvcgksPDkgfVVINQKGIDPPSLDLLAKEGIMALRRAK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    317 KTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQ 396
Cdd:TIGR02347 319 RRNMERLTLACGGEALNSVEDLTPECLGW-AGLVYETTIGEEKYTFIEECKNPKSCTILIKGPNDHTIAQIKDAVRDGLR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    397 VCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCE 476
Cdd:TIGR02347 398 AVKNAIEDKCVVPGAGAFEIAAYRHLKEYKKSVKGKAKLGVEAFANALLVIPKTLAENSGFDAQDTLVKLEDEHD-EGGE 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 6753320    477 TWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02347 477 VVGVDLNTGEPIDPEIKGIWDNYRVKKQLIQSATVIASQLLLVDEVM 523
TCP1_beta cd03336
TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in ...
9-524 4.79e-95

TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.


Pssm-ID: 239452 [Multi-domain]  Cd Length: 517  Bit Score: 298.86  E-value: 4.79e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:cd03336   1 ILKDGAQEEKGETARLSSFVGAIAIGDLVKTTLGPKGMDKILQsvGRSGGVTVTNDGATILKSIGVDNPAAKVLVDISKV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITTK 163
Cdd:cd03336  81 QDDEVGDGTTSVTVLAAELLREAEKLVAQKIHPQTIIEGYRMATAAAREALLSSAVDHSSDEeafREDLLNIARTTLSSK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  164 VISRWSSLACNIALDAVktvqFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLLDS 243
Cdd:cd03336 161 ILTQDKEHFAELAVDAV----LRLKGSGNLD---AIQIIKKLGGSLKDSYLDEGFLLDKKIGVNQPKR-IENAKILIANT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  244 SLEYKKgesqtdIEI----TREEDFTRILQMEE---EYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVR 316
Cdd:cd03336 233 PMDTDK------IKIfgakVRVDSTAKVAEIEEaekEKMKNKVEKILKHGINCFINRQLIYNYPEQLFADAGIMAIEHAD 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  317 KTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQ 396
Cdd:cd03336 307 FDGVERLALVTGGEIASTFDHPELVKLGT-CKLIEEIMIGEDKLIRFSGVAAGEACTIVLRGASQQILDEAERSLHDALC 385
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  397 VCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCe 476
Cdd:cd03336 386 VLAQTVKDTRVVLGGGCSEMLMAKAVEELAKKTPGKKSLAIEAFAKALRQLPTIIADNAGYDSAELVAQLRAAHYNGNT- 464
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*...
gi 6753320  477 TWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVS 524
Cdd:cd03336 465 TAGLDMRKGTVGDMKELGITESFKVKRQVLLSASEAAEMILRVDDIIK 512
chap_CCT_theta TIGR02346
T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the ...
26-523 1.71e-92

T-complex protein 1, theta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT alpha chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274087 [Multi-domain]  Cd Length: 531  Bit Score: 292.78  E-value: 1.71e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     26 NINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:TIGR02346  23 NIEACKELSQITRTSLGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKLLVMASEMQENEIGDGTNLVLVLAGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKIS--TPVDVNNREMMLSIINSSITTKVISRWSSLACNIAlDAVKTV 183
Cdd:TIGR02346 103 LNKAEELIRMGLHPSEIIKGYEMALKKAMEILEELVvwEVKDLRDKDELIKALKASISSKQYGNEDFLAQLVA-QACSTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    184 QFEENGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDvTHPRMRRyIKNPRIVLLDSSLEYKKGESQTDIEITREED 263
Cdd:TIGR02346 182 LPKNPQNFNVD---NIRVCKILGGSLSNSEVLKGMVFNRE-AEGSVKS-VKNAKVAVFSCPLDTATTETKGTVLIHNAEE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    264 FTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSR-----PEEL 338
Cdd:TIGR02346 257 LLNYSKGEENQIEAMIKAIADSGVNVIVTGGSVGDMALHYLNKYNIMVLKIPSKFELRRLCKTVGATPLPRlgaptPEEI 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    339 REDDVgtgaglLEIKKIGDEYFT-FITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMA 417
Cdd:TIGR02346 337 GYVDS------VYVSEIGGDKVTvFKQENGDSKISTIILRGSTDNLLDDIERAIDDGVNTVKALVKDGRLLPGAGATEIE 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    418 VAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHtQESCETWGVN--GETGTLVDMKELGI 495
Cdd:TIGR02346 411 LASRLTKYGEKLPGLDQYAIKKFAEAFEIIPRTLAENAGLNANEVIPKLYAAH-KKGNKSKGIDieAESDGVKDASEAGI 489
                         490       500
                  ....*....|....*....|....*...
gi 6753320    496 WEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02346 490 YDMLATKKWAIKLATEAAVTVLRVDQII 517
chaperonin_like cd03333
chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They ...
149-404 7.67e-78

chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. This superfamily also contains related domains from Fab1-like phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinases that only contain the intermediate and apical domains.


Pssm-ID: 239449 [Multi-domain]  Cd Length: 209  Bit Score: 243.91  E-value: 7.67e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  149 REMMLSIINSSITTKvISRWSSLACNIALDAVKTVQFEENgrkeIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPR 228
Cdd:cd03333   1 RELLLQVATTSLNSK-LSSWDDFLGKLVVDAVLKVGPDNR----MDDLGVIKVEKIPGGSLEDSELVVGVVFDKGYASPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  229 MRRYIKNPRIVLLDSSLEYkkgesqtdieitreedftrilqmeeeyihqlcediiqlkpdVVITEKGISDLAQHYLMRAN 308
Cdd:cd03333  76 MPKRLENAKILLLDCPLEY-----------------------------------------VVIAEKGIDDLALHYLAKAG 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  309 VTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVE 388
Cdd:cd03333 115 IMAVRRVKKEDLERIARATGATIVSSLEDLTPEDLGT-AELVEETKIGEEKLTFIEGCKGGKAATILLRGATEVELDEVK 193
                       250
                ....*....|....*.
gi 6753320  389 RNLQDAMQVCRNVLLD 404
Cdd:cd03333 194 RSLHDALCAVRAAVEE 209
chap_CCT_beta TIGR02341
T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the ...
9-523 6.28e-71

T-complex protein 1, beta subunit; Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.


Pssm-ID: 274082  Cd Length: 519  Bit Score: 235.91  E-value: 6.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320      9 VLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLL--DPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRT 86
Cdd:TIGR02341   2 IFKDGADEERAENARLSSFVGAIAIGDLVKSTLGPKGMDKILQssSSDASIMVTNDGATILKSIGVDNPAAKVLVDMSKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320     87 QDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNN---REMMLSIINSSITTK 163
Cdd:TIGR02341  82 QDDEVGDGTTSVTVLAAELLREAEKLINQKIHPQTIIAGYREATKAARDALLKSAVDNGSDEvkfRQDLMNIARTTLSSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    164 VISRWSSLACNIALDAVKTVQfeenGRKEIDikkYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRyIKNPRIVLLDS 243
Cdd:TIGR02341 162 ILSQHKDHFAQLAVDAVLRLK----GSGNLE---AIQIIKKLGGSLADSYLDEGFLLDKKIGVNQPKR-IENAKILIANT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    244 SLEYKKGES-QTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNR 322
Cdd:TIGR02341 234 GMDTDKVKIfGSRVRVDSTAKVAELEHAEKEKMKEKVEKILKHGINCFINRQLIYNYPEQLFADAGVMAIEHADFEGVER 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    323 IARACGARIVSRPEELREDDVGTgAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVL 402
Cdd:TIGR02341 314 LALVTGGEIVSTFDHPELVKLGS-CDLIEEIMIGEDKLLKFSGVKLGEACTIVLRGATQQILDEAERSLHDALCVLSQTV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    403 LDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTqESCETWGVNG 482
Cdd:TIGR02341 393 KESRTVLGGGCSEMLMSKAVTQEAQRTPGKEALAVEAFARALRQLPTIIADNAGFDSAELVAQLRAAHY-NGNTTMGLDM 471
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 6753320    483 ETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIV 523
Cdd:TIGR02341 472 NEGTIADMRQLGITESYKVKRAVVSSAAEAAEVILRVDNII 512
Fab1_TCP cd03334
TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. ...
167-392 1.23e-45

TCP-1 like domain of the eukaryotic phosphatidylinositol 3-phosphate (PtdIns3P) 5-kinase Fab1. Fab1p is important for vacuole size regulation, presumably by modulating PtdIns(3,5)P2 effector activity. In the human homolog p235/PIKfyve deletion of this domain leads to loss of catalytic activity. However no exact function this domain has been defined. In general, chaperonins are involved in productive folding of proteins.


Pssm-ID: 239450 [Multi-domain]  Cd Length: 261  Bit Score: 161.24  E-value: 1.23e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  167 RWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLE 246
Cdd:cd03334  18 SWLDILLPLVWKAASNVKPDVRAGDDMDIRQYVKIKKIPGGSPSDSEVVDGVVFTKNVAHKRMPSKIKNPRILLLQGPLE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  247 YKKGESQ-TDIEItreedftrILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIAR 325
Cdd:cd03334  98 YQRVENKlLSLDP--------VILQEKEYLKNLVSRIVALRPDVILVEKSVSRIAQDLLLEAGITLVLNVKPSVLERISR 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753320  326 ACGARIVSRPEEL-REDDVGTgAGLLEIKKIGDEY-----FTFITDCKDPKACTILLRGASKEILSEVERNLQ 392
Cdd:cd03334 170 CTGADIISSMDDLlTSPKLGT-CESFRVRTYVEEHgrsktLMFFEGCPKELGCTILLRGGDLEELKKVKRVVE 241
GroEL cd03344
GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They ...
30-517 9.50e-11

GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). With the aid of cochaperonin GroES, GroEL encapsulates non-native substrate proteins inside the cavity of the GroEL-ES complex and promotes folding by using energy derived from ATP hydrolysis.


Pssm-ID: 239460  Cd Length: 520  Bit Score: 64.01  E-value: 9.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   30 AKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEM 105
Cdd:cd03344  17 VNKLADAVKVTLGPKGRNVVIEKSFGSPKITKDGVTVAKEIELEDPfenmGAQLVKEVASKTNDVAGDGTTTATVLARAI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  106 LSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPvdVNNREMMLSI-INSSITTKVISRwsslacNIAlDAVKTVQ 184
Cdd:cd03344  97 IKEGLKAVAAGANPMDLKRGIEKAVEAVVEELKKLSKP--VKTKEEIAQVaTISANGDEEIGE------LIA-EAMEKVG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  185 FE-----ENGRK---EIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDssleyKKgesqtd 255
Cdd:cd03344 168 KDgvitvEEGKTletELEV-----VE----GMQFD----RGYLSPYFVTDPeKMEVELENPYILLTD-----KK------ 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  256 ieITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYL-------MRA--NVTAIR-----RVRKTDN 320
Cdd:cd03344 224 --ISSIQELLPIL-----------ELVAKAgRPLLIIAE----DVEGEALatlvvnkLRGglKVCAVKapgfgDRRKAML 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  321 NRIARACGARIVS-----RPEELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKActI-----LLRGASKEILSEVERN 390
Cdd:cd03344 287 EDIAILTGGTVISeelglKLEDVTLEDLGR-AKKVVVTK---DDTTIIGGAGDKAA--IkariaQIRKQIEETTSDYDKE 360
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320  391 --------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALtEKSKAMTGVEQWPYR 438
Cdd:cd03344 361 klqerlaklsggvavikvggatevelkekkdrVEDALNATR-AAVEEGIVPGGGVALLRASPAL-DKLKALNGDEKLGIE 438
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6753320  439 AVAQALEVIPRTLIQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLL 517
Cdd:cd03344 439 IVRRALEAPLRQIAENAGVD-----GSVVVEKVLESPDGFGYDAATGEYVDMIEAGIIDPTKVVRSALQNAASVASLLL 512
groEL PRK12850
chaperonin GroEL; Reviewed
32-545 1.37e-10

chaperonin GroEL; Reviewed


Pssm-ID: 237231  Cd Length: 544  Bit Score: 63.58  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12850  22 ILANAVKVTLGPKGRNVVLEKSFGAPRITKDGVTVAKEIELEDKfenmGAQMVKEVASKTNDLAGDGTTTATVLAQAIVR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEE 187
Cdd:PRK12850 102 EGAKLVAAGMNPMDLKRGIDLAVAAVVDELKKIAKKVTSSKEIAQVATISANGDESIGEMIAEAMDKVGKEGVITVEEAK 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   188 NGRKEIDIkkyarVEkipgGIIEDSCVLRGVMinkdVTHP-RMRRYIKNPRIVLldssleykkgesqTDIEITREEDFTR 266
Cdd:PRK12850 182 TLGTELDV-----VE----GMQFDRGYLSPYF----VTNPeKMRAELEDPYILL-------------HEKKISNLQDLLP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   267 ILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV--------------RKTDNNRIARACGARI 331
Cdd:PRK12850 236 IL-----------EAVVQSgRPLLIIAE----DVEGEALATLVVNKLRGGlksvavkapgfgdrRKAMLEDIAVLTGGQV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   332 VS-----RPEELREDDVGTGAGLLeikkIGDEYFTFITDCKDPK---ACTILLR-------------------------- 377
Cdd:PRK12850 301 ISedlgiKLENVTLDMLGRAKRVL----ITKENTTIIDGAGDKKnieARVKQIRaqieettsdydreklqerlaklaggv 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   378 -----GASKEI-LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQWPYRAVAQALEVIPRTL 451
Cdd:PRK12850 377 avirvGGATEVeVKEKKDRVDDALHATR-AAVEEGIVPGGGVALLRARSALRGL-KGANADETAGIDIVRRALEEPLRQI 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   452 IQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGD 531
Cdd:PRK12850 455 ATNAGFE-----GSVVVGKVAELPGNFGFNAQTGEYGDMVEAGIIDPAKVTRTALQDAASIAALLITTEAMVAEAPKKAA 529
                        570
                 ....*....|....
gi 6753320   532 DQNRQTGAPDAGQE 545
Cdd:PRK12850 530 AAAAGPGPGMGGMG 543
groEL PRK12851
chaperonin GroEL; Reviewed
17-530 1.64e-08

chaperonin GroEL; Reviewed


Pssm-ID: 171770  Cd Length: 541  Bit Score: 57.06  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    17 ESGRKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVG 92
Cdd:PRK12851  11 EAREKMLRG----VNILADAVKVTLGPKGRNVVIDKSFGAPTITNDGVTIAKEIELEDKfenmGAQMVREVASKTNDVAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    93 DGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIInSSITTKVISRWSSLA 172
Cdd:PRK12851  87 DGTTTATVLAQAIVREGAKAVAAGANPMDLKRGIDRAVAAVVEELKANARPVTTNAEIAQVATI-SANGDAEIGRLVAEA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   173 CN-IALDAVKTVQFEENGRKEIDIkkyarVEkipgGIIEDscvlRGVMINKDVTHP-RMRRYIKNPRIVLLDSsleykkg 250
Cdd:PRK12851 166 MEkVGNEGVITVEESKTAETELEV-----VE----GMQFD----RGYLSPYFVTDAdKMEAELEDPYILIHEK------- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   251 esqtdiEITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV-------------- 315
Cdd:PRK12851 226 ------KISNLQDLLPVL-----------EAVVQSgKPLLIIAE----DVEGEALATLVVNKLRGGlkvaavkapgfgdr 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   316 RKTDNNRIARACGARIVSRPEELREDDVgTGAGLLEIKK--IGDEYFTFITDCKDPKActilLRGASKEILSEVERN--- 390
Cdd:PRK12851 285 RKAMLEDIAILTGGTVISEDLGIKLENV-TLEQLGRAKKvvVEKENTTIIDGAGSKTE----IEGRVAQIRAQIEETtsd 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   391 ------------------------------------LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKsKAMTGVEQ 434
Cdd:PRK12851 360 ydreklqerlaklaggvavirvgastevevkekkdrVDDALHATR-AAVEEGIVPGGGVALLRAVKALDKL-ETANGDQR 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   435 WPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRakhtqESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAV 514
Cdd:PRK12851 438 TGVEIVRRALEAPVRQIAENAGAEGSVVVGKLR-----EKPGGYGFNAATNEYGDLYAQGVIDPVKVVRTALQNAASVAG 512
                        570
                 ....*....|....*.
gi 6753320   515 LLLRIDDIVSGHKKKG 530
Cdd:PRK12851 513 LLLTTEAMVAEKPKKE 528
PRK14104 PRK14104
chaperonin GroEL; Provisional
33-543 2.09e-08

chaperonin GroEL; Provisional


Pssm-ID: 172594  Cd Length: 546  Bit Score: 56.96  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    33 IADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSV 108
Cdd:PRK14104  23 LANAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKSADAAGDGTTTATVLAQAIVRE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   109 AEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEEN 188
Cdd:PRK14104 103 GAKSVAAGMNPMDLKRGIDLAVEAVVADLVKNSKKVTSNDEIAQVGTISANGDAEIGKFLADAMKKVGNEGVITVEEAKS 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   189 GRKEIDIKKYARVEK--IPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKK----------GESQTDI 256
Cdd:PRK14104 183 LETELDVVEGMQFDRgyISPYFVTNADKMRVEMDDAYILINEKKLSSLNELLPLLEAVVQTGKplvivaedveGEALATL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   257 EITREEDFTRILQMEEEYIHQLCEDIIQlkpDVVITEKG--ISDLAQHYLMRANVTAIRRVRKT----DNNRIARACG-- 328
Cdd:PRK14104 263 VVNRLRGGLKVAAVKAPGFGDRRKAMLQ---DIAILTGGqaISEDLGIKLENVTLQMLGRAKKVmidkENTTIVNGAGkk 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   329 ARIVSRPEELREddvgtgagllEIKKIGDEYFTFITDCKDPK----ACTILLRGASKEILSEVERNLQDAMQVCRnVLLD 404
Cdd:PRK14104 340 ADIEARVAQIKA----------QIEETTSDYDREKLQERLAKlaggVAVIRVGGATEVEVKERKDRVDDAMHATR-AAVE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   405 PQLVPGGGASEMAVAHAL----TEKSKAMTGVEqwpyrAVAQALEVIPRTLIQNCGASTirllTSLRAKHTQESCETWGV 480
Cdd:PRK14104 409 EGIVPGGGVALLRASEQLkgikTKNDDQKTGVE-----IVRKALSAPARQIAINAGEDG----SVIVGKILEKEQYSYGF 479
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753320   481 NGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAG 543
Cdd:PRK14104 480 DSQTGEYGNLVSKGIIDPTKVVRTAIQNAASVAALLITTEAMVAELPKKGGAGPAMPPGGGMG 542
PTZ00114 PTZ00114
Heat shock protein 60; Provisional
27-542 4.23e-08

Heat shock protein 60; Provisional


Pssm-ID: 185455  Cd Length: 555  Bit Score: 55.69  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    27 INAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPA----AKSMIEISRTQDEEVGDGTTSVIILA 102
Cdd:PTZ00114  28 LKGIERLADAVAVTLGPKGRNVIIEQEYGSPKITKDGVTVAKAIEFSDRFenvgAQLIRQVASKTNDKAGDGTTTATILA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   103 GEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPvdVNNREMMLSII-----NSSITTKVISRwsslacniAL 177
Cdd:PTZ00114 108 RAIFREGCKAVAAGLNPMDLKRGIDLAVKVVLESLKEQSRP--VKTKEDILNVAtisanGDVEIGSLIAD--------AM 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   178 DAV---KTVQFEENGRKEIDIKkyarvekipggIIEDSCVLRGVMINKDVTHPRMRRYI-KNPRIVLLDssleyKKGESQ 253
Cdd:PTZ00114 178 DKVgkdGTITVEDGKTLEDELE-----------VVEGMSFDRGYISPYFVTNEKTQKVElENPLILVTD-----KKISSI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   254 TDIeitreedfTRILqmeeEYIHQlcediiQLKPDVVITEKGISDLAQHYL---MRAN--VTAIR-----RVRKTDNNRI 323
Cdd:PTZ00114 242 QSI--------LPIL----EHAVK------NKRPLLIIAEDVEGEALQTLIinkLRGGlkVCAVKapgfgDNRKDILQDI 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   324 ARACGARIVSRPEELREDDVGTGAGLLEIKKI---GDEyfTFIT----DCKDPKACTILLRGA--------SKEIL---- 384
Cdd:PTZ00114 304 AVLTGATVVSEDNVGLKLDDFDPSMLGSAKKVtvtKDE--TVILtgggDKAEIKERVELLRSQierttseyDKEKLkerl 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   385 ---------------SEVERN-----LQDAMQVCRNVlLDPQLVPGGGAsemavahALTEKSKAMTGVEQWPYR------ 438
Cdd:PTZ00114 382 aklsggvavikvggaSEVEVNekkdrIEDALNATRAA-VEEGIVPGGGV-------ALLRASKLLDKLEEDNELtpdqrt 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   439 ---AVAQALEVIPRTLIQNCG---ASTIRLLtsLRAKHtqescETWGVNGETGTLVDMKELGIWEPLAVklqtYKTAVET 512
Cdd:PTZ00114 454 gvkIVRNALRLPTKQIAENAGvegAVVVEKI--LEKKD-----PSFGYDAQTGEYVNMFEAGIIDPTKV----VRSALVD 522
                        570       580       590
                 ....*....|....*....|....*....|....
gi 6753320   513 AV----LLLRIDDIVSGHKKKgDDQNRQTGAPDA 542
Cdd:PTZ00114 523 AAsvasLMLTTEAAIVDLPKE-KKKNKNSAAPPM 555
groEL PRK12852
chaperonin GroEL; Reviewed
32-529 1.25e-07

chaperonin GroEL; Reviewed


Pssm-ID: 237232  Cd Length: 545  Bit Score: 54.47  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQV----QHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12852  22 ILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVTVAKEIELedkfENMGAQMVREVASKTNDLAGDGTTTATVLAQAIVR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVqfEE 187
Cdd:PRK12852 102 EGAKAVAAGMNPMDLKRGIDIAVAAVVKDIEKRAKPVASSAEIAQVGTISANGDAAIGKMIAQAMQKVGNEGVITV--EE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   188 NGRKEIDIKkyarvekipggIIEDSCVLRGVMINKDVTHP-RMRRYIKNPRIVLLDSSL--------------------- 245
Cdd:PRK12852 180 NKSLETEVD-----------IVEGMKFDRGYLSPYFVTNAeKMTVELDDAYILLHEKKLsglqamlpvleavvqsgkpll 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   246 ---EYKKGESQTDIEITREEDFTRILQMEE----EYIHQLCEDIIQLKPDVVITEK-GISdlaqhyLMRANVTAIRRVRK 317
Cdd:PRK12852 249 iiaEDVEGEALATLVVNRLRGGLKVAAVKApgfgDRRKAMLEDIAILTGGQLISEDlGIK------LENVTLKMLGRAKK 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   318 T----DNNRIARACG--ARIVSRPEELREddvgtgagllEIKKIGDEYftfitD--------CKDPKACTILLRGASKEI 383
Cdd:PRK12852 323 VvidkENTTIVNGAGkkADIEARVGQIKA----------QIEETTSDY-----DreklqerlAKLAGGVAVIRVGGATEV 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   384 -LSEVERNLQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVeQWPYRAVAQALEVIPRTLIQNCGASTIRL 462
Cdd:PRK12852 388 eVKEKKDRVEDALNATR-AAVQEGIVPGGGVALLRAKKAVGRINNDNADV-QAGINIVLKALEAPIRQIAENAGVEGSIV 465
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6753320   463 LTSLRAKHTqescETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKK 529
Cdd:PRK12852 466 VGKILENKS----ETFGFDAQTEEYVDMVAKGIIDPAKVVRTALQDAASVAGLLVTTEAMVAELPKK 528
groEL PRK12849
chaperonin GroEL; Reviewed
32-543 1.80e-07

chaperonin GroEL; Reviewed


Pssm-ID: 237230  Cd Length: 542  Bit Score: 53.66  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    32 TIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGTTSVIILAGEMLS 107
Cdd:PRK12849  21 KLADAVKVTLGPKGRNVVIDKSFGAPTITKDGVSIAKEIELEDPfenlGAQLVKEVASKTNDVAGDGTTTATVLAQALVQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   108 VAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDvNNREM----MLSIINSSITTKVISRwsslacniALDAVKT- 182
Cdd:PRK12849 101 EGLKNVAAGANPMDLKRGIDKAVEAVVEELKALARPVS-GSEEIaqvaTISANGDEEIGELIAE--------AMEKVGKd 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   183 --VQFEENGRKEIDIKkyarvekipggiiedscVLRGVMINKD------VTHP-RMRRYIKNPRIVLLDssleyKKgesq 253
Cdd:PRK12849 172 gvITVEESKTLETELE-----------------VTEGMQFDRGylspyfVTDPeRMEAVLEDPLILLTD-----KK---- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   254 tdieITREEDFTRILqmeeeyihqlcEDIIQL-KPDVVITEkgisDLAQHYLMRANVTAIRRV--------------RKT 318
Cdd:PRK12849 226 ----ISSLQDLLPLL-----------EKVAQSgKPLLIIAE----DVEGEALATLVVNKLRGGlkvaavkapgfgdrRKA 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   319 DNNRIARACGARIVSRP-----EELREDDVGTgAGLLEIKKigdEYFTFITDCKDPKA---------------------- 371
Cdd:PRK12849 287 MLEDIAILTGGTVISEDlglklEEVTLDDLGR-AKRVTITK---DNTTIVDGAGDKEAiearvaqirrqieettsdydre 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   372 -------------CTILLRGAskeilSEVERN-----LQDAMQVCRnVLLDPQLVPGGGASEMAVAHALTEKSKA----M 429
Cdd:PRK12849 363 klqerlaklaggvAVIKVGAA-----TEVELKerkdrVEDALNATR-AAVEEGIVPGGGVALLRAAKALDELAGLngdqA 436
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320   430 TGVeqwpyRAVAQALEVIPRTLIQNCGAStirllTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTA 509
Cdd:PRK12849 437 AGV-----EIVRRALEAPLRQIAENAGLD-----GSVVVAKVLELEDGFGFNAATGEYGDLIAAGIIDPVKVTRSALQNA 506
                        570       580       590
                 ....*....|....*....|....*....|....
gi 6753320   510 VETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAG 543
Cdd:PRK12849 507 ASVAGLLLTTEALVADKPEEEDPPGGMGGMGGMG 540
PLN03167 PLN03167
Chaperonin-60 beta subunit; Provisional
20-145 5.82e-05

Chaperonin-60 beta subunit; Provisional


Pssm-ID: 215611 [Multi-domain]  Cd Length: 600  Bit Score: 45.69  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753320    20 RKVQSGninaAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHP----AAKSMIEISRTQDEEVGDGT 95
Cdd:PLN03167  69 KKLQAG----VNKLADLVGVTLGPKGRNVVLESKYGSPKIVNDGVTVAKEVELEDPveniGAKLVRQAAAKTNDLAGDGT 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 6753320    96 TSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVD 145
Cdd:PLN03167 145 TTSVVLAQGLIAEGVKVVAAGANPVQITRGIEKTAKALVKELKKMSKEVE 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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